ID   UTR1_YEAST              Reviewed;         530 AA.
AC   P21373; D6VWM0; E9P8Y8; Q54AD8;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 2.
DT   27-MAR-2024, entry version 184.
DE   RecName: Full=NAD(+) kinase;
DE            EC=2.7.1.23 {ECO:0000269|PubMed:11425472};
DE   AltName: Full=Unknown transcript 1 protein;
GN   Name=UTR1; OrderedLocusNames=YJR049C; ORFNames=J1655;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX   PubMed=11425472; DOI=10.1111/j.1574-6968.2001.tb10712.x;
RA   Kawai S., Mori S., Suzuki S., Murata K.;
RT   "Molecular cloning and identification of UTR1 of a yeast Saccharomyces
RT   cerevisiae as a gene encoding an NAD kinase.";
RL   FEMS Microbiol. Lett. 200:181-184(2001).
RN   [2]
RP   PRELIMINARY NUCLEOTIDE SEQUENCE.
RX   PubMed=2158927; DOI=10.1016/0378-1119(90)90297-5;
RA   Melnick L., Sherman F.;
RT   "Nucleotide sequence of the COR region: a cluster of six genes in the yeast
RT   Saccharomyces cerevisiae.";
RL   Gene 87:157-166(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7975898; DOI=10.1002/yea.320100611;
RA   Huang M.-E., Manus V., Chuat J.-C., Galibert F.;
RT   "Revised nucleotide sequence of the COR region of yeast Saccharomyces
RT   cerevisiae chromosome X.";
RL   Yeast 10:811-818(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [7]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499 AND SER-503, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499 AND SER-503, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Specifically phosphorylates NAD in the presence of ATP, dATP,
CC       or CTP as phosphoryl donors. {ECO:0000269|PubMed:11425472}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + NAD(+) = ADP + H(+) + NADP(+); Xref=Rhea:RHEA:18629,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:456216; EC=2.7.1.23;
CC         Evidence={ECO:0000269|PubMed:11425472};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18630;
CC         Evidence={ECO:0000269|PubMed:11425472};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.5 mM for NAD {ECO:0000269|PubMed:11425472};
CC         KM=0.6 mM for ATP {ECO:0000269|PubMed:11425472};
CC       pH dependence:
CC         Optimum pH is 8.0. {ECO:0000269|PubMed:11425472};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:11425472}.
CC   -!- INTERACTION:
CC       P21373; P32622: YEF1; NbExp=4; IntAct=EBI-20174, EBI-22350;
CC   -!- MISCELLANEOUS: Present with 5040 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the NAD kinase family. {ECO:0000305}.
CC   -!- CAUTION: Was briefly thought to be FRE2. {ECO:0000305}.
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DR   EMBL; AB044344; BAB83863.1; -; Genomic_DNA.
DR   EMBL; L26347; AAA62857.1; -; Genomic_DNA.
DR   EMBL; L36344; AAA88752.1; -; Genomic_DNA.
DR   EMBL; M37696; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z49549; CAA89577.1; -; Genomic_DNA.
DR   EMBL; AY692899; AAT92918.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08836.1; -; Genomic_DNA.
DR   PIR; S46589; S46589.
DR   RefSeq; NP_012583.1; NM_001181707.1.
DR   AlphaFoldDB; P21373; -.
DR   SMR; P21373; -.
DR   BioGRID; 33802; 96.
DR   DIP; DIP-4479N; -.
DR   IntAct; P21373; 5.
DR   MINT; P21373; -.
DR   STRING; 4932.YJR049C; -.
DR   iPTMnet; P21373; -.
DR   MaxQB; P21373; -.
DR   PaxDb; 4932-YJR049C; -.
DR   PeptideAtlas; P21373; -.
DR   EnsemblFungi; YJR049C_mRNA; YJR049C; YJR049C.
DR   GeneID; 853508; -.
DR   KEGG; sce:YJR049C; -.
DR   AGR; SGD:S000003810; -.
DR   SGD; S000003810; UTR1.
DR   VEuPathDB; FungiDB:YJR049C; -.
DR   eggNOG; KOG2178; Eukaryota.
DR   GeneTree; ENSGT00940000169386; -.
DR   HOGENOM; CLU_008831_1_5_1; -.
DR   InParanoid; P21373; -.
DR   OMA; MRMRLCC; -.
DR   OrthoDB; 455155at2759; -.
DR   BioCyc; MetaCyc:G3O-31684-MONOMER; -.
DR   BioCyc; YEAST:G3O-31684-MONOMER; -.
DR   BRENDA; 2.7.1.23; 984.
DR   BRENDA; 2.7.1.86; 984.
DR   Reactome; R-SCE-196807; Nicotinate metabolism.
DR   BioGRID-ORCS; 853508; 2 hits in 10 CRISPR screens.
DR   PRO; PR:P21373; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P21373; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003951; F:NAD+ kinase activity; IDA:SGD.
DR   GO; GO:0042736; F:NADH kinase activity; IDA:SGD.
DR   GO; GO:0006879; P:intracellular iron ion homeostasis; IMP:SGD.
DR   GO; GO:0019674; P:NAD metabolic process; IEA:InterPro.
DR   GO; GO:0006741; P:NADP biosynthetic process; IDA:SGD.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   HAMAP; MF_00361; NAD_kinase; 1.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
DR   InterPro; IPR017437; ATP-NAD_kinase_PpnK-typ_C.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   InterPro; IPR002504; NADK.
DR   PANTHER; PTHR20275; NAD KINASE; 1.
DR   PANTHER; PTHR20275:SF0; NAD KINASE; 1.
DR   Pfam; PF01513; NAD_kinase; 1.
DR   Pfam; PF20143; NAD_kinase_C; 1.
DR   SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; NAD; NADP; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   CHAIN           1..530
FT                   /note="NAD(+) kinase"
FT                   /id="PRO_0000120716"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          57..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          486..530
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..99
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         499
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         503
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   CONFLICT        337
FT                   /note="A -> V (in Ref. 6; AAT92918)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   530 AA;  59469 MW;  1BF4F01D7213B94B CRC64;
     MKENDMNNGV DKWVNEEDGR NDHHNNNNNL MKKAMMNNEQ IDRTQDIDNA KEMLRKISSE
     SSSRRSSLLN KDSSLVNGNA NSGGGTSING TRGSSKSSNT HFQYASTAYG VRMLSKDISN
     TKVELDVENL MIVTKLNDVS LYFLTRELVE WVLVHFPRVT VYVDSELKNS KKFAAGELCE
     DSKCRESRIK YWTKDFIREH DVFFDLVVTL GGDGTVLFVS SIFQRHVPPV MSFSLGSLGF
     LTNFKFEHFR EDLPRIMNHK IKTNLRLRLE CTIYRRHRPE VDPNTGKKIC VVEKLSTHHI
     LNEVTIDRGP SPFLSMLELY GDGSLMTVAQ ADGLIAATPT GSTAYSLSAG GSLVCPTVNA
     IALTPICPHA LSFRPIILPE SINLKVKVSM KSRAPAWAAF DGKDRIELQK GDFITICASP
     YAFPTVEASP DEFINSISRQ LNWNVREQQK SFTHILSQKN QEKYAHEANK VRNQAEPLEV
     IRDKYSLEAD ATKENNNGSD DESDDESVNC EACKLKPSSV PKPSQARFSV
//